ID   TRM3_EHV2               Reviewed;         686 AA.
AC   Q66632; Q66637;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Tripartite terminase subunit 3 {ECO:0000255|HAMAP-Rule:MF_04013};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04013};
DE   AltName: Full=Terminase large subunit {ECO:0000255|HAMAP-Rule:MF_04013};
GN   Name=TRM3 {ECO:0000255|HAMAP-Rule:MF_04013}; OrderedLocusNames=29a/29b;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Davison A.J.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the molecular motor that translocates viral
CC       genomic DNA in empty capsid during DNA packaging. Forms a tripartite
CC       terminase complex together with TRM1 and TRM2 in the host cytoplasm.
CC       Once the complex reaches the host nucleus, it interacts with the capsid
CC       portal vertex. This portal forms a ring in which genomic DNA is
CC       translocated into the capsid. TRM3 carries an RNase H-like nuclease
CC       activity that plays an important role for the cleavage of concatemeric
CC       viral DNA into unit length genomes. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC   -!- SUBUNIT: Interacts with the terminase subunits TRM1 and TRM2. Interacts
CC       with portal protein. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04013}.
CC       Note=Responsible for the nuclear localization of the two others
CC       subunits TRM1 and TRM2. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC   -!- SIMILARITY: Belongs to the herpesviridae TRM3 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04013}.
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DR   EMBL; U20824; AAC13821.2; -; Genomic_DNA.
DR   PIR; S55628; S55628.
DR   RefSeq; NP_042630.2; NC_001650.2.
DR   SMR; Q66632; -.
DR   PRIDE; Q66632; -.
DR   GeneID; 1461057; -.
DR   KEGG; vg:1461057; -.
DR   Proteomes; UP000007083; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.320; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_04013; HSV_TRM3; 1.
DR   InterPro; IPR003498; DNA_pack_C.
DR   InterPro; IPR038435; DNA_pack_C_sf.
DR   InterPro; IPR003499; DNA_pack_N.
DR   InterPro; IPR033663; HSV_TRM3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02499; DNA_pack_C; 1.
DR   Pfam; PF02500; DNA_pack_N; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Host nucleus; Hydrolase; Reference proteome;
KW   Viral genome packaging; Viral release from host cell.
FT   CHAIN           1..686
FT                   /note="Tripartite terminase subunit 3"
FT                   /id="PRO_0000406059"
FT   MOTIF           219..226
FT                   /note="Walker A motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   MOTIF           314..319
FT                   /note="Walker B motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        319
FT                   /note="For ATPase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        475
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        548
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT   ACT_SITE        660
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
SQ   SEQUENCE   686 AA;  76458 MW;  BC38099FB2A57A3A CRC64;
     MILSGKKRML LDNYKNARAP GGDDERDWVF DRPAIVTRRD KSDRMAHPYI GIIPRTNIYS
     AVLDSYCKSL NPVYKERIPP VLGTGRDVPV TPANVTGELA RAARALCGDL ASGDPEALVE
     FASAVQTQRT SRGCPVFREL SEFLVNLASF LNRCYSVKSD TIEPFQKQLI LHTFYFLISI
     KAPHAANTLF EVFKEYFGLF DMGREALQTF KQKSTVYLIP RRHGKTWIVV AIISMLLTSV
     ENIHVGYVAH QKHVANSVFA EIINTIYRWF PAKNVYIKKE NGTIMYTNEN RRPSTLMCAT
     CFNKNSIRGQ TFNLLYVDEA NFIKKDSLPS ILGFMLQKDA KIIFISSVNS SDQTTSFLYN
     LKNAKEKMLN VVNYVCPQHR EDFSLQESVV SCPCYRLHIP TYIAIDENIK DTTNLFMEGA
     FTTELMGDGA AATTQTNMHK VVGEPALVQF DLCRVDTGSP EAQRGLNPTL FLYVDPAYTN
     NTEASGTGMG AVVSMKNSDR CVVVGVEHFF LKELTGASSL QIASCAAALI RSLATLHPFV
     REAHVAIEGN SSQDSAVAIA TLLHERSPLP VKFLHHADKA TGVQWPMYIL GAEKARAFET
     FIYALNSNTL SCGQAIVSNT IKLSFDPVAY LIEQIRAIKC YPLKDGTVSY CAKHKGGSDD
     TLVAVVMAHY FATSDRHVFK NHMKQI